ID   TIM50_HUMAN             Reviewed;         353 AA.
AC   Q3ZCQ8; Q330K1; Q6QA00; Q96FJ5; Q96GY2; Q9H370;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   03-MAY-2023, entry version 165.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE   Flags: Precursor;
GN   Name=TIMM50; Synonyms=TIM50; ORFNames=PRO1512;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND INTERACTION WITH TIMM23.
RX   PubMed=15044455; DOI=10.1074/jbc.m402049200;
RA   Guo Y., Cheong N., Zhang Z., De Rose R., Deng Y., Farber S.A.,
RA   Fernandes-Alnemri T., Alnemri E.S.;
RT   "Tim50, a component of the mitochondrial translocator, regulates
RT   mitochondrial integrity and cell death.";
RL   J. Biol. Chem. 279:24813-24825(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Zheng H., Xie Y., Mao Y.;
RT   "Cloning of a novel splice variant of TIM50L.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND PARTIAL
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain, Eye, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-353.
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
RA   Gao F., Liu M., He F.;
RT   "Functional prediction of the coding sequences of 75 new genes deduced by
RT   analysis of cDNA clones from human fetal liver.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 98-113; 275-284; 285-295 AND 335-345, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 98-113, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [9]
RP   ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION (ISOFORM 2), RNA-BINDING
RP   (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   INTERACTION WITH COIL.
RX   PubMed=16008839; DOI=10.1186/1471-2121-6-29;
RA   Xu H., Somers Z.B., Robinson M.L. II, Hebert M.D.;
RT   "Tim50a, a nuclear isoform of the mitochondrial Tim50, interacts with
RT   proteins involved in snRNP biogenesis.";
RL   BMC Cell Biol. 6:29-29(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   INTERACTION WITH DNAJC15.
RX   PubMed=23263864; DOI=10.1093/hmg/dds541;
RA   Schusdziarra C., Blamowska M., Azem A., Hell K.;
RT   "Methylation-controlled J-protein MCJ acts in the import of proteins into
RT   human mitochondria.";
RL   Hum. Mol. Genet. 22:1348-1357(2013).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-341, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [14]
RP   INVOLVEMENT IN MGCA9, AND VARIANTS MGCA9 TRP-114 AND MET-149.
RX   PubMed=27573165; DOI=10.1111/cge.12855;
RG   NISC Intramural Sequencing;
RA   Shahrour M.A., Staretz-Chacham O., Dayan D., Stephen J., Weech A.,
RA   Damseh N., Pri Chen H., Edvardson S., Mazaheri S., Saada A.,
RA   Hershkovitz E., Shaag A., Huizing M., Abu-Libdeh B., Gahl W.A., Azem A.,
RA   Anikster Y., Vilboux T., Elpeleg O., Malicdan M.C.;
RT   "Mitochondrial epileptic encephalopathy, 3-methylglutaconic aciduria and
RT   variable complex V deficiency associated with TIMM50 mutations.";
RL   Clin. Genet. 91:690-696(2017).
CC   -!- FUNCTION: Essential component of the TIM23 complex, a complex that
CC       mediates the translocation of transit peptide-containing proteins
CC       across the mitochondrial inner membrane. Has some phosphatase activity
CC       in vitro; however such activity may not be relevant in vivo.
CC       {ECO:0000269|PubMed:15044455}.
CC   -!- FUNCTION: [Isoform 2]: May participate in the release of snRNPs and SMN
CC       from the Cajal body. {ECO:0000269|PubMed:16008839}.
CC   -!- SUBUNIT: Component of the TIM23 complex at least composed of TIMM23,
CC       TIMM17 (TIMM17A or TIMM17B) and TIMM50; within this complex, directly
CC       interacts with TIMM23 (PubMed:15044455). The complex interacts with the
CC       TIMM44 component of the PAM complex and with DNAJC15 (PubMed:23263864).
CC       {ECO:0000269|PubMed:15044455, ECO:0000269|PubMed:23263864}.
CC   -!- SUBUNIT: [Isoform 2]: Interacts with COIL and snRNPs (PubMed:16008839).
CC       {ECO:0000269|PubMed:16008839}.
CC   -!- INTERACTION:
CC       Q3ZCQ8; P10398: ARAF; NbExp=4; IntAct=EBI-355175, EBI-365961;
CC       Q3ZCQ8; P04049: RAF1; NbExp=6; IntAct=EBI-355175, EBI-365996;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:15044455}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:15044455}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus speckle
CC       {ECO:0000269|PubMed:16008839}. Note=Nuclear and enriched in speckles
CC       with snRNPs. {ECO:0000269|PubMed:16008839}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3ZCQ8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Tim50a;
CC         IsoId=Q3ZCQ8-2; Sequence=VSP_016389;
CC       Name=3;
CC         IsoId=Q3ZCQ8-3; Sequence=VSP_047682, VSP_047683;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC       brain, kidney and liver (at protein level).
CC       {ECO:0000269|PubMed:15044455, ECO:0000269|PubMed:16008839}.
CC   -!- DOMAIN: The FCP1 homology domain does not contain the canonical D-x-D-
CC       x-[TV] active site, suggesting that it probably does not display
CC       phosphatase activity in vivo.
CC   -!- DISEASE: 3-methylglutaconic aciduria 9 (MGCA9) [MIM:617698]: An
CC       autosomal recessive disease characterized by early-onset seizures,
CC       severely delayed psychomotor development and intellectual disability.
CC       Patients have hypotonia or spasticity, and laboratory investigations
CC       show increased serum lactate and 3-methylglutaconic aciduria.
CC       {ECO:0000269|PubMed:27573165}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG35534.1; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305};
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DR   EMBL; AY551341; AAT01208.1; -; mRNA.
DR   EMBL; AY444561; AAS68537.1; -; mRNA.
DR   EMBL; AC011500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009072; AAH09072.1; -; mRNA.
DR   EMBL; BC010736; AAH10736.1; -; mRNA.
DR   EMBL; BC050082; AAH50082.1; -; mRNA.
DR   EMBL; BC121146; AAI21147.1; -; mRNA.
DR   EMBL; AF130109; AAG35534.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS33023.2; -. [Q3ZCQ8-1]
DR   RefSeq; NP_001001563.1; NM_001001563.3. [Q3ZCQ8-1]
DR   RefSeq; NP_001316488.1; NM_001329559.1. [Q3ZCQ8-3]
DR   AlphaFoldDB; Q3ZCQ8; -.
DR   SMR; Q3ZCQ8; -.
DR   BioGRID; 124961; 241.
DR   ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
DR   ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR   CORUM; Q3ZCQ8; -.
DR   DIP; DIP-34058N; -.
DR   IntAct; Q3ZCQ8; 108.
DR   MINT; Q3ZCQ8; -.
DR   STRING; 9606.ENSP00000445806; -.
DR   ChEMBL; CHEMBL4295842; -.
DR   DEPOD; TIMM50; -.
DR   GlyGen; Q3ZCQ8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3ZCQ8; -.
DR   PhosphoSitePlus; Q3ZCQ8; -.
DR   SwissPalm; Q3ZCQ8; -.
DR   BioMuta; TIMM50; -.
DR   DMDM; 83305924; -.
DR   EPD; Q3ZCQ8; -.
DR   jPOST; Q3ZCQ8; -.
DR   MassIVE; Q3ZCQ8; -.
DR   MaxQB; Q3ZCQ8; -.
DR   PaxDb; Q3ZCQ8; -.
DR   PeptideAtlas; Q3ZCQ8; -.
DR   ProteomicsDB; 61635; -.
DR   ProteomicsDB; 61909; -. [Q3ZCQ8-1]
DR   ProteomicsDB; 61910; -. [Q3ZCQ8-2]
DR   TopDownProteomics; Q3ZCQ8-1; -. [Q3ZCQ8-1]
DR   TopDownProteomics; Q3ZCQ8-2; -. [Q3ZCQ8-2]
DR   Antibodypedia; 30377; 190 antibodies from 32 providers.
DR   DNASU; 92609; -.
DR   Ensembl; ENST00000544017.5; ENSP00000445806.2; ENSG00000105197.11. [Q3ZCQ8-2]
DR   Ensembl; ENST00000607714.6; ENSP00000475531.1; ENSG00000105197.11. [Q3ZCQ8-1]
DR   GeneID; 92609; -.
DR   KEGG; hsa:92609; -.
DR   MANE-Select; ENST00000607714.6; ENSP00000475531.1; NM_001001563.5; NP_001001563.2.
DR   UCSC; uc002olu.1; human. [Q3ZCQ8-1]
DR   AGR; HGNC:23656; -.
DR   CTD; 92609; -.
DR   DisGeNET; 92609; -.
DR   GeneCards; TIMM50; -.
DR   HGNC; HGNC:23656; TIMM50.
DR   HPA; ENSG00000105197; Low tissue specificity.
DR   MalaCards; TIMM50; -.
DR   MIM; 607381; gene.
DR   MIM; 617698; phenotype.
DR   neXtProt; NX_Q3ZCQ8; -.
DR   OpenTargets; ENSG00000105197; -.
DR   Orphanet; 505216; 3-methylglutaconic aciduria type 9.
DR   PharmGKB; PA134902846; -.
DR   VEuPathDB; HostDB:ENSG00000105197; -.
DR   eggNOG; KOG2832; Eukaryota.
DR   GeneTree; ENSGT01040000240503; -.
DR   HOGENOM; CLU_048293_1_1_1; -.
DR   InParanoid; Q3ZCQ8; -.
DR   OrthoDB; 11362at2759; -.
DR   PhylomeDB; Q3ZCQ8; -.
DR   TreeFam; TF106198; -.
DR   PathwayCommons; Q3ZCQ8; -.
DR   Reactome; R-HSA-1268020; Mitochondrial protein import.
DR   SignaLink; Q3ZCQ8; -.
DR   SIGNOR; Q3ZCQ8; -.
DR   BioGRID-ORCS; 92609; 144 hits in 1186 CRISPR screens.
DR   ChiTaRS; TIMM50; human.
DR   GeneWiki; TIMM50; -.
DR   GenomeRNAi; 92609; -.
DR   Pharos; Q3ZCQ8; Tbio.
DR   PRO; PR:Q3ZCQ8; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q3ZCQ8; protein.
DR   Bgee; ENSG00000105197; Expressed in left testis and 173 other tissues.
DR   ExpressionAtlas; Q3ZCQ8; baseline and differential.
DR   Genevisible; Q3ZCQ8; HS.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IPI:UniProtKB.
DR   GO; GO:0005134; F:interleukin-2 receptor binding; IDA:MGI.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:ComplexPortal.
DR   GO; GO:0007006; P:mitochondrial membrane organization; IMP:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:MGI.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR12210:SF3; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM50; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disease variant; Epilepsy;
KW   Intellectual disability; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; RNA-binding; Transit peptide; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..353
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM50"
FT                   /id="PRO_0000043115"
FT   TOPO_DOM        45..65
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..353
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          143..286
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          25..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..11
FT                   /note="MAASAAVFSRL -> MVPRFLMSSTM (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_047682"
FT   VAR_SEQ         1
FT                   /note="M -> MASALSLGNKCDPFLRCVLCRGGGALQGPRGRGPDDFESQLSPPGSA
FT                   RRLVRSKRACGNPPDAFGLSRASVHPPLPRVSIGCSSGPGRAKRERVGGAAWRQRKM
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_016389"
FT   VAR_SEQ         12..124
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_047683"
FT   VARIANT         114
FT                   /note="R -> W (in MGCA9; unknown pathological significance;
FT                   dbSNP:rs1300848445)"
FT                   /evidence="ECO:0000269|PubMed:27573165"
FT                   /id="VAR_078568"
FT   VARIANT         149
FT                   /note="T -> M (in MGCA9; unknown pathological significance;
FT                   dbSNP:rs1244226820)"
FT                   /evidence="ECO:0000269|PubMed:27573165"
FT                   /id="VAR_078569"
SQ   SEQUENCE   353 AA;  39646 MW;  524EB9989BBF6988 CRC64;
     MAASAAVFSR LRSGLRLGSR GLCTRLATPP RRAPDQAAEI GSRGSTKAQG PQQQPGSEGP
     SYAKKVALWL AGLLGAGGTV SVVYIFGNNP VDENGAKIPD EFDNDPILVQ QLRRTYKYFK
     DYRQMIIEPT SPCLLPDPLQ EPYYQPPYTL VLELTGVLLH PEWSLATGWR FKKRPGIETL
     FQQLAPLYEI VIFTSETGMT AFPLIDSVDP HGFISYRLFR DATRYMDGHH VKDISCLNRD
     PARVVVVDCK KEAFRLQPYN GVALRPWDGN SDDRVLLDLS AFLKTIALNG VEDVRTVLEH
     YALEDDPLAA FKQRQSRLEQ EEQQRLAELS KSNKQNLFLG SLTSRLWPRS KQP
//